Ubiquitous activation of the Nipah virus fusion protein does not require a basic amino acid at the cleavage site
about
Identification of a broad-spectrum antiviral small molecule against severe acute respiratory syndrome coronavirus and Ebola, Hendra, and Nipah viruses by using a novel high-throughput screening assayModes of paramyxovirus fusion: a Henipavirus perspectiveHenipavirus mediated membrane fusion, virus entry and targeted therapeuticsCo-assembly of viral envelope glycoproteins regulates their polarized sorting in neuronsRole of sequence and structure of the Hendra fusion protein fusion peptide in membrane fusion.Hendra and Nipah viruses: different and dangerous.ANP32B is a nuclear target of henipavirus M proteins.Envelope targeting: hemagglutinin attachment specificity rather than fusion protein cleavage-activation restricts Tupaia paramyxovirus tropism.Modification of the trypsin-dependent cleavage activation site of the human metapneumovirus fusion protein to be trypsin independent does not increase replication or spread in rodents or nonhuman primates.Analysis of cathepsin and furin proteolytic enzymes involved in viral fusion protein activation in cells of the bat reservoir host.Complete genome sequence of avian paramyxovirus type 7 (strain Tennessee) and comparison with other paramyxoviruses.Mutation of the f-protein cleavage site of avian paramyxovirus type 7 results in furin cleavage, fusion promotion, and increased replication in vitro but not increased replication, tissue tropism, or virulence in chickens.Structure and stabilization of the Hendra virus F glycoprotein in its prefusion formNipah virus entry and egress from polarized epithelial cellsComplete sequence of the genome of avian paramyxovirus type 2 (strain Yucaipa) and comparison with other paramyxoviruses.Preventing Cleavage of the Respiratory Syncytial Virus Attachment Protein in Vero Cells Rescues the Infectivity of Progeny Virus for Primary Human Airway Cultures.Activation of the Nipah virus fusion protein in MDCK cells is mediated by cathepsin B within the endosome-recycling compartment.Endocytosis of the Nipah virus glycoproteinsNipah virus infection and glycoprotein targeting in endothelial cells.Ephrin-B2 expression critically influences Nipah virus infection independent of its cytoplasmic tail.Side chain packing below the fusion peptide strongly modulates triggering of the Hendra virus F proteinSelective receptor expression restricts Nipah virus infection of endothelial cells.Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein.Endocytosis plays a critical role in proteolytic processing of the Hendra virus fusion proteinTyrosine residues in the cytoplasmic domains affect sorting and fusion activity of the Nipah virus glycoproteins in polarized epithelial cells.The nipah virus fusion protein is cleaved within the endosomal compartment.
P2860
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P2860
Ubiquitous activation of the Nipah virus fusion protein does not require a basic amino acid at the cleavage site
description
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2004年の論文
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2004年学术文章
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name
Ubiquitous activation of the N ...... mino acid at the cleavage site
@en
Ubiquitous activation of the N ...... ino acid at the cleavage site.
@nl
type
label
Ubiquitous activation of the N ...... mino acid at the cleavage site
@en
Ubiquitous activation of the N ...... ino acid at the cleavage site.
@nl
prefLabel
Ubiquitous activation of the N ...... mino acid at the cleavage site
@en
Ubiquitous activation of the N ...... ino acid at the cleavage site.
@nl
P2093
P2860
P50
P1433
P1476
Ubiquitous activation of the N ...... mino acid at the cleavage site
@en
P2093
Andrea Maisner
Markus Czub
Sandra Diederich
P2860
P304
P356
10.1128/JVI.78.18.9705-9712.2004
P407
P577
2004-09-01T00:00:00Z